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Protein

Cyclin-L2

Gene

Ccnl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Transcriptional regulator which participates in regulating the pre-mRNA splicing process. Also modulates the expression of critical apoptotic factor, leading to cell apoptosis (By similarity).By similarity

GO - Biological processi

  1. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. RNA processing Source: InterPro
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-L2
Alternative name(s):
Cyclin Ania-6b
Paneth cell-enhanced expression protein
Short name:
PCEE
Gene namesi
Name:Ccnl2
Synonyms:Ania6b
ORF Names:MNCb-5160
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1927119. Ccnl2.

Subcellular locationi

Nucleus speckle By similarity

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB-SubCell
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 518518Cyclin-L2PRO_0000080488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei328 – 3281PhosphoserineBy similarity
Modified residuei335 – 3351PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei348 – 3481PhosphoserineBy similarity
Modified residuei366 – 3661PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9JJA7.
PaxDbiQ9JJA7.
PRIDEiQ9JJA7.

PTM databases

PhosphoSiteiQ9JJA7.

Expressioni

Gene expression databases

BgeeiQ9JJA7.
CleanExiMM_CCNL2.
GenevestigatoriQ9JJA7.

Interactioni

Subunit structurei

Interacts with CDK11A, CDK11B, CDK12, CDK13, SFRS2, SFRS7 and POLR2A, the hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II.1 Publication

Protein-protein interaction databases

IntActiQ9JJA7. 1 interaction.
MINTiMINT-4129894.
STRINGi10090.ENSMUSP00000030944.

Structurei

3D structure databases

ProteinModelPortaliQ9JJA7.
SMRiQ9JJA7. Positions 50-286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 183103Cyclin-like 1Add
BLAST
Regioni196 – 28085Cyclin-like 2Add
BLAST
Regioni382 – 42039RSAdd
BLAST

Domaini

Contains a RS region (arginine-serine dipeptide repeat) within the C-terminal domain which is the hallmark of the SR family of splicing factors. This region probably plays a role in protein-protein interactions (By similarity).By similarity

Sequence similaritiesi

Belongs to the cyclin family. Cyclin L subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5333.
GeneTreeiENSGT00760000119191.
HOVERGENiHBG056044.
InParanoidiQ9JJA7.
OMAiLDQEYVN.
OrthoDBiEOG7K9K34.
PhylomeDBiQ9JJA7.
TreeFamiTF101011.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR015429. Cyclin_C/H/T/L.
IPR017060. Cyclin_L.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10026. PTHR10026. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036580. Cyclin_L. 1 hit.
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9JJA7-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAAAGAAG LMAPASAACS SGSAGAAPGS QGVLIGDRLY SGVLITLENC
60 70 80 90 100
LLPDDKLRFT PSMSSGLDVD TETGLRVVGC ELIQAAGILL RLPQVAMATG
110 120 130 140 150
QVLFQRFFYT KSFVKHSMEH VSMACVHLAS KIEEAPRRIR DVINVFHRLR
160 170 180 190 200
HLREKKKPVP LVLDQEYVNL KNQIIKAERR VLKELGFCVH VKHPHKIIVM
210 220 230 240 250
YLQVLECERN QHLVQTAWNY MNDSLRTDVF VRFQPESIAC ACIYLAARTL
260 270 280 290 300
EIPLPNRPHW FLLFGATEEE IQEICFKILQ LYTRKKVDLT HLESEVEKRK
310 320 330 340 350
HAIEEAKARA KGLLPGTAPG LDSAAGFSPA PKLESPKEGK GGKPSPPSGK
360 370 380 390 400
SAKRKMEGPK KAQGHSPVNG LLKGQESRSQ SRSREQSYSR SPSRSASPKR
410 420 430 440 450
RKSDSGSTSG GSKSQSRSRS RSDSPPRQVH RGAPYKGSEV RGSRKSKDCK
460 470 480 490 500
YLTQKPHKSR SRSSSRSRSR SRERTDNSGK YKKKSHYYRD QRRERSRSYE
510
RTGHRYERDH PGHSRHRR
Length:518
Mass (Da):58,005
Last modified:October 1, 2000 - v1
Checksum:iC93AEE68682CDBA5
GO
Isoform 2 (identifier: Q9JJA7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-224: NYMNDS → VASEGK
     225-518: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:224
Mass (Da):24,578
Checksum:i744000F7C7D3084E
GO
Isoform 3 (identifier: Q9JJA7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-518: Missing.

Note: No experimental confirmation available.

Show »
Length:218
Mass (Da):24,006
Checksum:i584E197FA66E601D
GO

Sequence cautioni

The sequence AAC52504.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAC52504.1 differs from that shown. Reason: Erroneous termination at position 519. Translated as stop.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161S → A in BAE41413. (PubMed:16141072)Curated
Sequence conflicti16 – 161S → A in BAE33556. (PubMed:16141072)Curated
Sequence conflicti16 – 161S → A in EDL15040. 1 PublicationCurated
Sequence conflicti16 – 161S → A in AAI32296. (PubMed:15489334)Curated
Sequence conflicti131 – 1311K → R in BAC26255. (PubMed:16141072)Curated
Sequence conflicti282 – 2821Y → F in AAH03773. (PubMed:15489334)Curated
Sequence conflicti317 – 3171T → S in EDL15040. 1 PublicationCurated
Sequence conflicti317 – 3171T → S in AAH03773. (PubMed:15489334)Curated
Sequence conflicti317 – 3171T → S in AAI32296. (PubMed:15489334)Curated
Sequence conflicti334 – 3341E → VE in AAH03773. (PubMed:15489334)Curated
Sequence conflicti334 – 3341E → VE in AAH83055. (PubMed:15489334)Curated
Sequence conflicti334 – 3341E → VE in AAC52504. (PubMed:8838426)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei219 – 518300Missing in isoform 3. 1 PublicationVSP_016133Add
BLAST
Alternative sequencei219 – 2246NYMNDS → VASEGK in isoform 2. 3 PublicationsVSP_016134
Alternative sequencei225 – 518294Missing in isoform 2. 3 PublicationsVSP_016135Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF211859 mRNA. Translation: AAF23011.1.
AY337018 mRNA. Translation: AAQ01205.1.
AB041605 mRNA. Translation: BAA95088.1.
AK007552 mRNA. Translation: BAB25103.1.
AK029033 mRNA. Translation: BAC26255.1.
AK048244 mRNA. Translation: BAE43334.1.
AK156037 mRNA. Translation: BAE33556.1.
AK169857 mRNA. Translation: BAE41413.1.
AL670236 Genomic DNA. Translation: CAM18388.1.
CH466594 Genomic DNA. Translation: EDL15040.1.
BC003773 mRNA. Translation: AAH03773.2.
BC023747 mRNA. No translation available.
BC083055 mRNA. Translation: AAH83055.1.
BC132295 mRNA. Translation: AAI32296.1.
U37351 mRNA. Translation: AAC52504.1. Sequence problems.
CCDSiCCDS19042.1. [Q9JJA7-1]
RefSeqiNP_997561.1. NM_207678.1. [Q9JJA7-1]
UniGeneiMm.23492.

Genome annotation databases

EnsembliENSMUST00000030944; ENSMUSP00000030944; ENSMUSG00000029068. [Q9JJA7-1]
GeneIDi56036.
KEGGimmu:56036.
UCSCiuc008wev.1. mouse. [Q9JJA7-3]
uc008wew.1. mouse. [Q9JJA7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF211859 mRNA. Translation: AAF23011.1.
AY337018 mRNA. Translation: AAQ01205.1.
AB041605 mRNA. Translation: BAA95088.1.
AK007552 mRNA. Translation: BAB25103.1.
AK029033 mRNA. Translation: BAC26255.1.
AK048244 mRNA. Translation: BAE43334.1.
AK156037 mRNA. Translation: BAE33556.1.
AK169857 mRNA. Translation: BAE41413.1.
AL670236 Genomic DNA. Translation: CAM18388.1.
CH466594 Genomic DNA. Translation: EDL15040.1.
BC003773 mRNA. Translation: AAH03773.2.
BC023747 mRNA. No translation available.
BC083055 mRNA. Translation: AAH83055.1.
BC132295 mRNA. Translation: AAI32296.1.
U37351 mRNA. Translation: AAC52504.1. Sequence problems.
CCDSiCCDS19042.1. [Q9JJA7-1]
RefSeqiNP_997561.1. NM_207678.1. [Q9JJA7-1]
UniGeneiMm.23492.

3D structure databases

ProteinModelPortaliQ9JJA7.
SMRiQ9JJA7. Positions 50-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JJA7. 1 interaction.
MINTiMINT-4129894.
STRINGi10090.ENSMUSP00000030944.

PTM databases

PhosphoSiteiQ9JJA7.

Proteomic databases

MaxQBiQ9JJA7.
PaxDbiQ9JJA7.
PRIDEiQ9JJA7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030944; ENSMUSP00000030944; ENSMUSG00000029068. [Q9JJA7-1]
GeneIDi56036.
KEGGimmu:56036.
UCSCiuc008wev.1. mouse. [Q9JJA7-3]
uc008wew.1. mouse. [Q9JJA7-1]

Organism-specific databases

CTDi81669.
MGIiMGI:1927119. Ccnl2.

Phylogenomic databases

eggNOGiCOG5333.
GeneTreeiENSGT00760000119191.
HOVERGENiHBG056044.
InParanoidiQ9JJA7.
OMAiLDQEYVN.
OrthoDBiEOG7K9K34.
PhylomeDBiQ9JJA7.
TreeFamiTF101011.

Miscellaneous databases

NextBioi311796.
PROiQ9JJA7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJA7.
CleanExiMM_CCNL2.
GenevestigatoriQ9JJA7.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR015429. Cyclin_C/H/T/L.
IPR017060. Cyclin_L.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR10026. PTHR10026. 1 hit.
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036580. Cyclin_L. 1 hit.
SMARTiSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dopamine and glutamate induce distinct striatal splice forms of Ania-6, an RNA polymerase II-associated cyclin."
    Berke J.D., Sgambato V., Zhu P.-P., Lavoie B., Vincent M., Krause M., Hyman S.E.
    Neuron 32:277-287(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6.
  2. "Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells."
    Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.
    J. Biol. Chem. 279:11639-11648(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  3. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J and NOD.
    Tissue: Head, Pancreas, Skin and Spleen.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: FVB/N.
    Tissue: Brain and Mammary gland.
  8. "Patterns of gene expression along the crypt-villus axis in mouse jejunal epithelium."
    Cheng H., Bjerknes M.
    Anat. Rec. 244:78-94(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 321-518.
    Strain: BALB/c.
    Tissue: Jejunal epithelium.
  9. "CDK13/CDC2L5 interacts with L-type cyclins and regulates alternative splicing."
    Chen H.H., Wong Y.H., Geneviere A.M., Fann M.J.
    Biochem. Biophys. Res. Commun. 354:735-740(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION CDK13.

Entry informationi

Entry nameiCCNL2_MOUSE
AccessioniPrimary (citable) accession number: Q9JJA7
Secondary accession number(s): A2AD95
, A2RSY2, Q5XK66, Q60995, Q8C136, Q8CIJ8, Q99L73, Q9QXH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 1, 2000
Last modified: February 4, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.